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| | <StructureSection load='1uhn' size='340' side='right'caption='[[1uhn]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='1uhn' size='340' side='right'caption='[[1uhn]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1uhn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UHN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UHN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1uhn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UHN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UHN FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1aui|1aui]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1uhn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uhn OCA], [https://pdbe.org/1uhn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uhn RCSB], [https://www.ebi.ac.uk/pdbsum/1uhn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uhn ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1uhn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uhn OCA], [https://pdbe.org/1uhn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uhn RCSB], [https://www.ebi.ac.uk/pdbsum/1uhn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uhn ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/CNBL2_ARATH CNBL2_ARATH]] Acts as a calcium sensor. CBL proteins interact with CIPK serine-threonine protein kinases. Binding of a CBL protein to the regulatory NAF domain of a CIPK protein lead to the activation of the kinase in a calcium-dependent manner. Binds four calcium ions per subunit. Mediates the activation of AKT1 by CIPK proteins (CIPK6, CIPK16, and CIPK23) in response to low potassium conditions and in the context of stomatal movement. Mediates the inactivation of the proton pump AHA2 by CIPK11. Probably involved in regulating signaling responses to abscisic acid.<ref>PMID:17483306</ref> <ref>PMID:17898163</ref> <ref>PMID:22547024</ref>
| + | [https://www.uniprot.org/uniprot/CNBL2_ARATH CNBL2_ARATH] Acts as a calcium sensor. CBL proteins interact with CIPK serine-threonine protein kinases. Binding of a CBL protein to the regulatory NAF domain of a CIPK protein lead to the activation of the kinase in a calcium-dependent manner. Binds four calcium ions per subunit. Mediates the activation of AKT1 by CIPK proteins (CIPK6, CIPK16, and CIPK23) in response to low potassium conditions and in the context of stomatal movement. Mediates the inactivation of the proton pump AHA2 by CIPK11. Probably involved in regulating signaling responses to abscisic acid.<ref>PMID:17483306</ref> <ref>PMID:17898163</ref> <ref>PMID:22547024</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Arath]] | + | [[Category: Arabidopsis thaliana]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hashimoto, H]] | + | [[Category: Hashimoto H]] |
| - | [[Category: Koizumi, N]] | + | [[Category: Koizumi N]] |
| - | [[Category: Nagae, M]] | + | [[Category: Nagae M]] |
| - | [[Category: Nozawa, A]] | + | [[Category: Nozawa A]] |
| - | [[Category: Sano, H]] | + | [[Category: Sano H]] |
| - | [[Category: Sato, M]] | + | [[Category: Sato M]] |
| - | [[Category: Shimizu, T]] | + | [[Category: Shimizu T]] |
| - | [[Category: Calcium binding protein]]
| + | |
| - | [[Category: Metal binding protein]]
| + | |
| Structural highlights
Function
CNBL2_ARATH Acts as a calcium sensor. CBL proteins interact with CIPK serine-threonine protein kinases. Binding of a CBL protein to the regulatory NAF domain of a CIPK protein lead to the activation of the kinase in a calcium-dependent manner. Binds four calcium ions per subunit. Mediates the activation of AKT1 by CIPK proteins (CIPK6, CIPK16, and CIPK23) in response to low potassium conditions and in the context of stomatal movement. Mediates the inactivation of the proton pump AHA2 by CIPK11. Probably involved in regulating signaling responses to abscisic acid.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Arabidopsis thaliana calcineurin B-like protein (AtCBL2) is a member of a recently identified family of calcineurin B-like calcium-binding proteins in A. thaliana. The crystal structure of AtCBL2 has been determined at 2.1 A resolution. The protein forms a compact alpha-helical structure with two pairs of EF-hand motifs. The structure is similar in overall folding topology to the structures of calcineurin B and neuronal calcium sensor 1, but differs significantly in local conformation. The two calcium ions are coordinated in the first and fourth EF-hand motifs, whereas the second and third EF-hand motifs are maintained in the open form by internal hydrogen bonding without coordination of calcium ions. Both a possible site and a possible mechanism for the target binding to AtCBL2 are discussed based on the three-dimensional structure.
The crystal structure of the novel calcium-binding protein AtCBL2 from Arabidopsis thaliana.,Nagae M, Nozawa A, Koizumi N, Sano H, Hashimoto H, Sato M, Shimizu T J Biol Chem. 2003 Oct 24;278(43):42240-6. Epub 2003 Jul 19. PMID:12871972[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Fuglsang AT, Guo Y, Cuin TA, Qiu Q, Song C, Kristiansen KA, Bych K, Schulz A, Shabala S, Schumaker KS, Palmgren MG, Zhu JK. Arabidopsis protein kinase PKS5 inhibits the plasma membrane H+ -ATPase by preventing interaction with 14-3-3 protein. Plant Cell. 2007 May;19(5):1617-34. Epub 2007 May 4. PMID:17483306 doi:http://dx.doi.org/10.1105/tpc.105.035626
- ↑ Lee SC, Lan WZ, Kim BG, Li L, Cheong YH, Pandey GK, Lu G, Buchanan BB, Luan S. A protein phosphorylation/dephosphorylation network regulates a plant potassium channel. Proc Natl Acad Sci U S A. 2007 Oct 2;104(40):15959-64. Epub 2007 Sep 26. PMID:17898163 doi:http://dx.doi.org/0707912104
- ↑ Batistic O, Rehers M, Akerman A, Schlucking K, Steinhorst L, Yalovsky S, Kudla J. S-acylation-dependent association of the calcium sensor CBL2 with the vacuolar membrane is essential for proper abscisic acid responses. Cell Res. 2012 Jul;22(7):1155-68. doi: 10.1038/cr.2012.71. Epub 2012 May 1. PMID:22547024 doi:http://dx.doi.org/10.1038/cr.2012.71
- ↑ Nagae M, Nozawa A, Koizumi N, Sano H, Hashimoto H, Sato M, Shimizu T. The crystal structure of the novel calcium-binding protein AtCBL2 from Arabidopsis thaliana. J Biol Chem. 2003 Oct 24;278(43):42240-6. Epub 2003 Jul 19. PMID:12871972 doi:http://dx.doi.org/10.1074/jbc.M303630200
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